MYO5A_RAT
ID MYO5A_RAT Reviewed; 1828 AA.
AC Q9QYF3;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Unconventional myosin-Va;
DE AltName: Full=Dilute myosin heavy chain, non-muscle;
GN Name=Myo5a;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10920234; DOI=10.1007/s003350010121;
RA Futaki S., Takagishi Y., Hayashi Y., Ohmori S., Kanou Y., Inouye M.,
RA Oda S., Seo H., Iwaikawa Y., Murata Y.;
RT "Identification of a novel myosin-Va mutation in an ataxic mutant rat,
RT dilute-opisthotonus.";
RL Mamm. Genome 11:649-655(2000).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1032, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
RN [3]
RP FUNCTION, AND INTERACTION WITH RIPL2.
RX PubMed=19812310; DOI=10.1242/jcs.050344;
RA Lise M.F., Srivastava D.P., Arstikaitis P., Lett R.L., Sheta R.,
RA Viswanathan V., Penzes P., O'Connor T.P., El-Husseini A.;
RT "Myosin-Va-interacting protein, RILPL2, controls cell shape and neuronal
RT morphogenesis via Rac signaling.";
RL J. Cell Sci. 122:3810-3821(2009).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-600; SER-1425 AND SER-1625,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Processive actin-based motor that can move in large steps
CC approximating the 36-nm pseudo-repeat of the actin filament. Involved
CC in melanosome transport. Also mediates the transport of vesicles to the
CC plasma membrane. May also be required for some polarization process
CC involved in dendrite formation. {ECO:0000269|PubMed:19812310}.
CC -!- SUBUNIT: May be a homodimer, which associates with multiple calmodulin
CC or myosin light chains (By similarity). Interacts with RIPL2, the
CC interaction is required for its role in dendrite formation
CC (PubMed:19812310). Interacts with MLPH. Interacts with SYTL4 (By
CC similarity). Interacts with MYRIP (By similarity). Interacts with
CC RAB10; mediates the transport to the plasma membrane of SLC2A4/GLUT4
CC storage vesicles (By similarity). Interacts with FMR1; this interaction
CC occurs in association with polyribosome (By similarity).
CC {ECO:0000250|UniProtKB:Q99104, ECO:0000269|PubMed:19812310}.
CC -!- DISEASE: Note=Defects in Myo5a are a cause of Dilute-opisthotonus
CC (dop). Dop rats have diluted coat color and are occasionally associated
CC with severe neurological disorders.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000305}.
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DR EMBL; AB035736; BAA88350.1; -; mRNA.
DR RefSeq; NP_071514.1; NM_022178.1.
DR AlphaFoldDB; Q9QYF3; -.
DR SMR; Q9QYF3; -.
DR BioGRID; 247098; 8.
DR IntAct; Q9QYF3; 3.
DR MINT; Q9QYF3; -.
DR iPTMnet; Q9QYF3; -.
DR PhosphoSitePlus; Q9QYF3; -.
DR jPOST; Q9QYF3; -.
DR PRIDE; Q9QYF3; -.
DR GeneID; 25017; -.
DR KEGG; rno:25017; -.
DR UCSC; RGD:3143; rat.
DR CTD; 4644; -.
DR RGD; 3143; Myo5a.
DR InParanoid; Q9QYF3; -.
DR OrthoDB; 311886at2759; -.
DR PhylomeDB; Q9QYF3; -.
DR Reactome; R-RNO-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR PRO; PR:Q9QYF3; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0042641; C:actomyosin; ISO:RGD.
DR GO; GO:0042642; C:actomyosin, myosin complex part; IDA:RGD.
DR GO; GO:0030424; C:axon; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0032433; C:filopodium tip; ISO:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0005794; C:Golgi apparatus; ISO:RGD.
DR GO; GO:0032593; C:insulin-responsive compartment; ISS:UniProtKB.
DR GO; GO:0005882; C:intermediate filament; ISO:RGD.
DR GO; GO:0042470; C:melanosome; ISO:RGD.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0016459; C:myosin complex; ISO:RGD.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0001750; C:photoreceptor outer segment; ISO:RGD.
DR GO; GO:0098794; C:postsynapse; ISO:RGD.
DR GO; GO:0098871; C:postsynaptic actin cytoskeleton; IDA:SynGO.
DR GO; GO:0055037; C:recycling endosome; IDA:RGD.
DR GO; GO:1990904; C:ribonucleoprotein complex; IDA:RGD.
DR GO; GO:0001726; C:ruffle; ISO:RGD.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IDA:SynGO.
DR GO; GO:0030141; C:secretory granule; IDA:RGD.
DR GO; GO:0005790; C:smooth endoplasmic reticulum; ISO:RGD.
DR GO; GO:0008021; C:synaptic vesicle; IDA:RGD.
DR GO; GO:0016461; C:unconventional myosin complex; ISO:RGD.
DR GO; GO:0003779; F:actin binding; ISO:RGD.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IDA:RGD.
DR GO; GO:0043008; F:ATP-dependent protein binding; IPI:RGD.
DR GO; GO:0005509; F:calcium ion binding; ISO:RGD.
DR GO; GO:0048306; F:calcium-dependent protein binding; IPI:RGD.
DR GO; GO:0005516; F:calmodulin binding; ISO:RGD.
DR GO; GO:0003774; F:cytoskeletal motor activity; IMP:RGD.
DR GO; GO:0097718; F:disordered domain specific binding; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0000146; F:microfilament motor activity; IDA:RGD.
DR GO; GO:0019901; F:protein kinase binding; IPI:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0031267; F:small GTPase binding; ISO:RGD.
DR GO; GO:0000149; F:SNARE binding; IPI:RGD.
DR GO; GO:0017075; F:syntaxin-1 binding; IPI:RGD.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0030048; P:actin filament-based movement; IDA:RGD.
DR GO; GO:0099640; P:axo-dendritic protein transport; IMP:RGD.
DR GO; GO:0032869; P:cellular response to insulin stimulus; ISS:UniProtKB.
DR GO; GO:0007268; P:chemical synaptic transmission; ISO:RGD.
DR GO; GO:0048066; P:developmental pigmentation; ISO:RGD.
DR GO; GO:0042417; P:dopamine metabolic process; IMP:RGD.
DR GO; GO:0051643; P:endoplasmic reticulum localization; ISO:RGD.
DR GO; GO:0099089; P:establishment of endoplasmic reticulum localization to postsynapse; ISO:RGD.
DR GO; GO:0006887; P:exocytosis; ISO:RGD.
DR GO; GO:0048820; P:hair follicle maturation; ISO:RGD.
DR GO; GO:0030073; P:insulin secretion; ISO:RGD.
DR GO; GO:0031987; P:locomotion involved in locomotory behavior; ISO:RGD.
DR GO; GO:0042759; P:long-chain fatty acid biosynthetic process; ISO:RGD.
DR GO; GO:0016236; P:macroautophagy; IMP:RGD.
DR GO; GO:0042438; P:melanin biosynthetic process; ISO:RGD.
DR GO; GO:0006582; P:melanin metabolic process; ISO:RGD.
DR GO; GO:0030318; P:melanocyte differentiation; ISO:RGD.
DR GO; GO:0032400; P:melanosome localization; ISO:RGD.
DR GO; GO:0032402; P:melanosome transport; ISO:RGD.
DR GO; GO:0042552; P:myelination; ISO:RGD.
DR GO; GO:0033602; P:negative regulation of dopamine secretion; IMP:RGD.
DR GO; GO:0051967; P:negative regulation of synaptic transmission, glutamatergic; IMP:RGD.
DR GO; GO:0050885; P:neuromuscular process controlling balance; ISO:RGD.
DR GO; GO:0042476; P:odontogenesis; ISO:RGD.
DR GO; GO:0043473; P:pigmentation; IMP:MGI.
DR GO; GO:1900078; P:positive regulation of cellular response to insulin stimulus; IMP:RGD.
DR GO; GO:1904960; P:positive regulation of cytochrome-c oxidase activity; IMP:RGD.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; IMP:RGD.
DR GO; GO:1904754; P:positive regulation of vascular associated smooth muscle cell migration; IMP:RGD.
DR GO; GO:0006892; P:post-Golgi vesicle-mediated transport; ISO:RGD.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISS:UniProtKB.
DR GO; GO:0065003; P:protein-containing complex assembly; IMP:RGD.
DR GO; GO:0150103; P:reactive gliosis; IMP:RGD.
DR GO; GO:0017157; P:regulation of exocytosis; IMP:RGD.
DR GO; GO:0031585; P:regulation of inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity; ISO:RGD.
DR GO; GO:0099566; P:regulation of postsynaptic cytosolic calcium ion concentration; ISO:RGD.
DR GO; GO:0032252; P:secretory granule localization; IDA:RGD.
DR GO; GO:0050808; P:synapse organization; ISO:RGD.
DR GO; GO:0030050; P:vesicle transport along actin filament; IMP:RGD.
DR GO; GO:0016192; P:vesicle-mediated transport; ISS:UniProtKB.
DR GO; GO:0007601; P:visual perception; ISO:RGD.
DR CDD; cd15478; Myo5a_CBD; 1.
DR CDD; cd01380; MYSc_Myo5; 1.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR002710; Dilute_dom.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR037988; Myo5a_CBD.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR004009; Myosin_N.
DR InterPro; IPR036103; MYSc_Myo5.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF01843; DIL; 1.
DR Pfam; PF00612; IQ; 6.
DR Pfam; PF00063; Myosin_head; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM01132; DIL; 1.
DR SMART; SM00015; IQ; 6.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF52540; SSF52540; 3.
DR PROSITE; PS51126; DILUTE; 1.
DR PROSITE; PS50096; IQ; 6.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS51844; SH3_LIKE; 1.
PE 1: Evidence at protein level;
KW Acetylation; Actin-binding; ATP-binding; Calmodulin-binding; Coiled coil;
KW Motor protein; Myosin; Nucleotide-binding; Phosphoprotein;
KW Protein transport; Reference proteome; Repeat; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4I1"
FT CHAIN 2..1828
FT /note="Unconventional myosin-Va"
FT /id="PRO_0000123458"
FT DOMAIN 8..60
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01190"
FT DOMAIN 69..763
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 766..788
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 789..813
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 814..836
FT /note="IQ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 837..861
FT /note="IQ 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 862..884
FT /note="IQ 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 885..914
FT /note="IQ 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 1507..1783
FT /note="Dilute"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00503"
FT REGION 599..633
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 643..665
FT /note="Actin-binding"
FT /evidence="ECO:0000255"
FT REGION 1105..1147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 914..1239
FT /evidence="ECO:0000255"
FT COILED 1314..1418
FT /evidence="ECO:0000255"
FT COMPBIAS 599..613
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 163..170
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4I1"
FT MOD_RES 600
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1032
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16641100"
FT MOD_RES 1425
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1625
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1733
FT /note="Phosphothreonine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1828 AA; 211764 MW; 5B3DE1C89AE36123 CRC64;
MAASELYTKF ARVWIPDPEE VWKSAELLKD YKPGDKVLLL HLEEGKDLEY RLDPKTSELP
HLRNPDILVG ENDLTALSYL HEPAVLHNLR VRFIDSKLIY TYCGIVLVAI NPYEQLPIYG
EDIINAYSGQ NMGDMDPHIF AVAEEAYKQM ARDERNQSII VSGESGAGKT VSAKYAMRYF
ATVSGSASEA NVEEKVLASN PIMESIGNAK TTRNDNSSRF GKYIEIGFDK RYRIIGANMR
TYLLEKSRVV FQAEEERNYH IFYQLCASAK LPEFKMLRLG NADSFHYTKQ GGSPMIEGVD
DAKEMAHTRQ ACTLLGISES YQMGIFRILA GILHLGNVGF ASRDSDSCTI PPKHEPLIIF
CDLMGVDYEE MCHWLCHRKL ATATETYIKP ISKLQATNAR DALAKHIYAK LFNWIVGHVN
QALHSAVKQH SFIGVLDIYG FETFEINSFE QFCINYANEK LQQQFNMHVF KLEQEEYMKE
QIPWTLIDFY DNQPCINLIE SKLGILDLLD EECKMPKGTD DTWAQKLYNT HLNKCALFEK
PRMSNKAFII KHFADKVEYQ CEGFLEKNKD TVFEEQIKVL KSSKFKMLPE LFQDDEKAIS
PTSATSSGRT PLTRVPVKPT KGRPGQTAKE HKKTVGLQFR NSLHLLMETL NATTPHYVRC
IKPNDFKFPF TFDEKRAVQQ LRACGVLETI RISAAGFPSR WTYQEFFSRY RVLMKQKDVL
GDRKQTCQNV LEKLILDKDK YQFGKTKIFF RAGQVAYLEK LRADKLRAAC IRIQKTIRGW
LLRKRYLCMQ RAAITVQRYV RGYQARCYAK FLRRTKAATT IQKYWRMYVV RRKYKIRRAA
TIVLQSYLRG YLARNRYRKI LREHKAVIIQ KRVRGWLART HYKRTMKAII YLQCCFRRMM
AKRELKKLKI EARSVERYKK LHIGMENKIM QLQRKVDEQN KDYKCLMEKL TNLEGVYNSE
TEKLRNDVER LQLSEEEAKV ATGRVLSLQE EIAKLRKDLE QTRSEKKSIE ERADKYKQET
EQLVSNLKEE NTLLKQEKET LNHLMVEQAK EMTETMERKL VEETKQLELD LNDERLRYQN
LLNEFSRLEE RYDDLKEEMT LMLNVPKPGH KRTDSTHSSN ESEYTFSSEF AETEDIAPRT
EEPTEKKVPL DMSLFLKLQK RVTELGQEKQ LMQDELDRKE EQVLRSKAKG GERPQIRGAE
LGYESLKRQE LESENKKLKN ELNELRKALS EKSAPEVNAP GAPAYRVLME QLTAVSEELD
VRKEEVLILR SQLVSQKEAI QPKDDKNTMT DSTILLEDVQ KMKDKGEIAQ AYIGLKETNR
LLESQLQSQK RSHENEAEAL RGEIQSLKEE NNRQQQLLAQ NLQLPPEARI EASLQHEITR
LTNENLDLME QLEKQDKTVR KLKKQLKVFA KKIGELEVGQ MENISPGQII DEPIRPVNIP
RKGKDFQGML EYKREDEQKL VKNLILELKP RGVAVNLISG LPAYILFMCV RHADYLDDDQ
KVRSLLTSTI NSIKKVLKKR GDDFETVSFW LSNTCRFLHC LKQYSGEEGF MKHNTSRQNE
HCLTNFDLAE YRQVLSDLAI QIYQQLVRVL ENILQPMIVS GMLEHETIQG VSGVKPTGLR
KRTSSIADEG TYTLDSILRQ LNSFHSVMCQ HGMDPELIKQ VVKQMFYIVG AITLNNLLLR
KDMCSWSKGM QIRYNVSQLE EWLRDKNLMN SGAKETLEPL IQAAQLLQVK KKTDDDAEAI
CSMCNALTTA QIVKVLNLYT PVNEFEERVS VSFIRTIQVR LRDRKDSPQL LMDAKHIFPV
TFPFNPSSLA LETIQIPASL GLGFIARV
